8X1A
Crystal structure of periplasmic G6P binding protein VcA0625
This is a non-PDB format compatible entry.
Summary for 8X1A
Entry DOI | 10.2210/pdb8x1a/pdb |
Descriptor | Iron(III) ABC transporter, periplasmic iron-compound-binding protein, 6-O-phosphono-alpha-D-glucopyranose (3 entities in total) |
Functional Keywords | vibrio cholerae, abc transporter, periplasmic ligand binding protein, sugar binding protein |
Biological source | Vibrio cholerae O395 |
Total number of polymer chains | 1 |
Total formula weight | 35673.82 |
Authors | Dasgupta, J.,Saha, I. (deposition date: 2023-11-06, release date: 2024-04-17, Last modification date: 2024-11-13) |
Primary citation | Saha, I.,Ghosh, B.,Dasgupta, J. Structural insights in to the atypical type-I ABC Glucose-6-phosphate importer VCA0625-27 of Vibrio cholerae. Biochem.Biophys.Res.Commun., 716:150030-150030, 2024 Cited by PubMed Abstract: Sugar phosphates are potential sources of carbon and phosphate for bacteria. Despite that the process of internalization of Glucose-6-Phosphate (G6P) through plasma membrane remained elusive in several bacteria. VCA0625-27, made of periplasmic ligand binding protein (PLBP) VCA0625, an atypical monomeric permease VCA0626, and a cytosolic ATPase VCA0627, recently emerged as hexose-6-phosphate uptake system of Vibrio cholerae. Here we report high resolution crystal structure of VCA0625 in G6P bound state that largely resembles AfuA of Actinobacillus pleuropneumoniae. MD simulations on VCA0625 in apo and G6P bound states unraveled an 'open to close' and swinging bi-lobal motions, which are diminished upon G6P binding. Mutagenesis followed by biochemical assays on VCA0625 underscored that R34 works as gateway to bind G6P. Although VCA0627 binds ATP, it is ATPase deficient in the absence of VCA0625 and VCA0626, which is a signature phenomenon of type-I ABC importer. Further, modeling, docking and systematic sequence analysis allowed us to envisage the existence of similar atypical type-I G6P importer with fused monomeric permease in 27 other gram-negative bacteria. PubMed: 38704889DOI: 10.1016/j.bbrc.2024.150030 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.604 Å) |
Structure validation
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